3b95
From Proteopedia
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'''EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 2)''' | '''EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 2)''' | ||
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[[Category: Collins, R E.]] | [[Category: Collins, R E.]] | ||
[[Category: Horton, J R.]] | [[Category: Horton, J R.]] | ||
- | [[Category: | + | [[Category: Ank repeat]] |
- | [[Category: | + | [[Category: Ankyrin repeat]] |
- | [[Category: | + | [[Category: Methyltransferase]] |
- | [[Category: | + | [[Category: Transferase]] |
- | [[Category: | + | [[Category: Transferase/structual protein complex]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:32:20 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 17:32, 4 May 2008
EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 2)
Contents |
Overview
Histone modifications have important roles in transcriptional control, mitosis and heterochromatin formation. G9a and G9a-like protein (GLP) are euchromatin-associated methyltransferases that repress transcription by mono- and dimethylating histone H3 at Lys9 (H3K9). Here we demonstrate that the ankyrin repeat domains of G9a and GLP bind with strong preference to N-terminal H3 peptides containing mono- or dimethyl K9. X-ray crystallography revealed the basis for recognition of the methylated lysine by a partial hydrophobic cage with three tryptophans and one acidic residue. Substitution of key residues in the cage eliminated the H3 tail interaction. Hence, G9a and GLP contain a new type of methyllysine binding module (the ankyrin repeat domains) and are the first examples of protein (histone) methyltransferases harboring in a single polypeptide the activities that generate and read the same epigenetic mark.
Disease
Known disease associated with this structure: Chromosome 9q subtelomeric deletion syndrome OMIM:[607001]
About this Structure
3B95 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules., Collins RE, Northrop JP, Horton JR, Lee DY, Zhang X, Stallcup MR, Cheng X, Nat Struct Mol Biol. 2008 Mar;15(3):245-50. Epub 2008 Feb 10. PMID:18264113 Page seeded by OCA on Sun May 4 20:32:20 2008